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Добірка наукової літератури з теми "Elongation factor 1A"

Автор: Grafiati
Опубліковано: 10 грудня 2022
Оновлено: 28 січня 2023

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Статті в журналах з теми "Elongation factor 1A"

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Belyi, Y., R. Niggeweg, B. Opitz, M. Vogelsgesang, S. Hippenstiel, M. Wilm, and K. Aktories. "Legionella pneumophila glucosyltransferase inhibits host elongation factor 1A." Proceedings of the National Academy of Sciences 103, no. 45 (October 26, 2006): 16953–58. http://dx.doi.org/10.1073/pnas.0601562103.

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Beckelman, Brenna C., Xueyan Zhou, C. Dirk Keene, and Tao Ma. "Impaired Eukaryotic Elongation Factor 1A Expression in Alzheimer's Disease." Neurodegenerative Diseases 16, no. 1-2 (November 10, 2015): 39–43. http://dx.doi.org/10.1159/000438925.

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3

Hamey, Joshua J., and Marc R. Wilkins. "Methylation of Elongation Factor 1A: Where, Who, and Why?" Trends in Biochemical Sciences 43, no. 3 (March 2018): 211–23. http://dx.doi.org/10.1016/j.tibs.2018.01.004.

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Candido-Silva, J. A., and N. Monesi. "Bradysia hygida (Diptera, Sciaridae) presents two eukaryotic Elongation Factor 1A gene homologues: partial characterization of the eukaryotic Elongation Factor 1A-F1 gene." Brazilian Journal of Medical and Biological Research 43, no. 5 (May 2010): 437–44. http://dx.doi.org/10.1590/s0100-879x2010007500029.

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Ursin, Virginia M., Jonathan M. Irvine, William R. Hiatt, and Christine K. Shewmaker. "Developmental Analysis of Elongation Factor-1a Expression in Transgenic Tobacco." Plant Cell 3, no. 6 (June 1991): 583. http://dx.doi.org/10.2307/3869187.

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Lukash, T. O. "Eukaryotic elongation factor 1A disintegrates aggregates of phenylalanyl-tRNA synthetase." Biopolymers and Cell 22, no. 1 (January 20, 2006): 29–32. http://dx.doi.org/10.7124/bc.000717.

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7

Zobel-Thropp, Pamela, Melody C. Yang, Lorenzo Machado, and Steven Clarke. "A Novel Post-translational Modification of Yeast Elongation Factor 1A." Journal of Biological Chemistry 275, no. 47 (September 5, 2000): 37150–58. http://dx.doi.org/10.1074/jbc.m001005200.

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Budkevich, T. V., A. A. Timchenko, E. I. Tiktopulo, B. S. Negrutskii, V. F. Shalak, Z. M. Petrushenko, V. L. Aksenov, et al. "Extended Conformation of Mammalian Translation Elongation Factor 1A in Solution†." Biochemistry 41, no. 51 (December 2002): 15342–49. http://dx.doi.org/10.1021/bi026495h.

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Itagaki, Keisuke, Toshihiko Naito, Ryota Iwakiri, Makoto Haga, Shougo Miura, Yohei Saito, Toshiyuki Owaki, et al. "Eukaryotic Translation Elongation Factor 1A Induces Anoikis by Triggering Cell Detachment." Journal of Biological Chemistry 287, no. 19 (March 7, 2012): 16037–46. http://dx.doi.org/10.1074/jbc.m111.308122.

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Mansilla, F., C. R. Knudsen, and B. F. C. Clark. "Mutational analysis of Glu272 in elongation factor 1A of E. coli." FEBS Letters 429, no. 3 (June 16, 1998): 417–20. http://dx.doi.org/10.1016/s0014-5793(98)00646-2.

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Більше джерел

Дисертації з теми "Elongation factor 1A"

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Többen, Udo. "A novel function for the eukaryotic translation elongation factor 1A." [S.l. : s.n.], 2004. http://deposit.ddb.de/cgi-bin/dokserv?idn=972338101.

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Bourbeau, Denis 1971. "Characterization of S1eEF1A-2 function, a sister gene of elongation factor 1A-1." Thesis, McGill University, 2001. http://digitool.Library.McGill.CA:80/R/?func=dbin-jump-full&object_id=36876.

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Анотація:
Protein translation in mammalian cells can be divided into three stages: initiation, elongation, and termination, which require several factors. The peptide elongation factor 1A (eEF1A-1), which was formerly referred to as eEF-1alpha, is a guanosine triphosphate (GTP) binding protein and it is responsible for bringing aminoacyl-tRNA to the ribosomes in the process of protein synthesis. The S1/eEF1A-2 factor also referred to as S1, is an isoform of eEF1A-1. Both proteins are expressed from two distinct genes and share 92% identity in their amino acid sequences. Besides the tissue specific expression S1/eEF1A-2, little is known about the functions of the S1/cEF1A-2 isoform. The objective of this thesis is Thus to investigate the function of the newly discovered peptide elongation factor A-2. The fact that the eEF1A-1 and Sl/eEF1A-2 isoforms' expressions are inversely controlled during development, led me to hypothesise that S1/eEF1A-2 down-regulates eEF1A-1 expression. The goal of the present work was to establish whether S1/eEF1A-2 is responsible for the down-regulation of eEF1A-1 during development in brain, heart and muscle, and how its expression influences cell biology. To address this hypothesis, several cell lines were transduced with an adenovirus expressing S1/eEF1A-2. Ectopic expression of S1/eEF1A-2 in the cardiomyocyte cell line H9c2 led to a down-regulation of eEF1A-1. Similar findings were observed in neuron-differentiated P19 cells, Hela cells, and WI38 cells. Furthermore, S1/eEF1A-2 expression led to a reduced rate of peptide elongation as demonstrated by ribosomal transit time analyses. My data suggest that S1/eEF1A-2 may compete with eEF1A-1 in peptide elongation, leading to a reduced elongation rate, which could be responsible for the relative down-regulation of eEF1A-1. This would imply that terminally differentiated cells, which express high levels of S1/eEF1A-2 (neurones, myocytes, and cardiomyocytes), have a distinct kinetic of peptide elonga
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Davies, Faith Cathryn Joy. "Role of eEF1A isoforms in neuritogenesis and epilepsy." Thesis, University of Edinburgh, 2017. http://hdl.handle.net/1842/23588.

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Eukaryotic Elongation Factor 1A (eEF1A) exists in two forms in vertebrates. The first form, eEF1A1, is expressed ubiquitously throughout development but is downregulated postdevelopmentally and replaced with eEF1A2, an isoform sharing 92% amino acid identity, in neurons and muscle. The primary function of eEF1A is to recruit amino-acylated tRNAs in a GTP-dependent manner to the A site of the ribosome during protein translation, but it also has non-canonical roles in the cell, some of which are isoform dependent. The reasons for the cell-type dependent switch from eEF1A1 to eEF1A2 are poorly understood. The first aim of this project was to examine the role played by eEF1A isoforms in neuritogenesis. To do this I used RNAi to significantly reduce expression of one or other isoform in neuronal cells and measure the effects this had on neurite outgrowth. Neurite outgrowth was significantly reduced in cells depleted of eEF1A1, but not eEF1A2. The complete loss of eEF1A2 is fatal, as has been demonstrated in the wasted mouse, an eEF1A2-null model characterised by muscle wastage, neurodegeneration and death at 4 weeks of age. Mice heterozygous for the wasted mutation have normal motor function. Recent work has found that heterozygous missense mutations in eEF1A2 can cause epilepsy and intellectual disability. It is not yet known whether the seven different de novo mutations identified to date confer loss or gain of function – a crucial piece of information required before possible treatments can be sought. The second aim of this project therefore was to investigate the role of eEF1A2 in epilepsy and intellectual disability. I achieved this by using CRISPR in two ways; firstly to model one of the mutations, D252H, in vitro in a neuronal cell line, and secondly to model another of the mutations, G70S, in vivo. No mice that recapitulated the human disease condition of EEF1A2G70S/+ were obtained however, due to the error-prone nature of the non-homologous end joining repair pathway activated by CRISPR-mediated DNA cleavage, 17 of the 35 mice born were found to be homozygous nulls at the Eef1a2 locus. Nine of these had fatal audiogenic seizures caused by sudden loud noises within the animal unit. Three mice were Eef1a2G70S/- and one Eef1a2G70S/G70S but these nonetheless showed a wasted phenotype, indicating that this mutant form of eEF1A2 has compromised function, at least in terms of translation elongation. Whether it has a toxic function ca not yet be known, but the severity of the phenotype in the G70S homozygous animal could suggest a gain of function. In in vitro experiments with exogenous eEF1A2 carrying the epilepsy-causing mutation R423C, protein expression of the mutant construct in immortalised cell lines was significantly higher when cotransfected with the wildtype construct, which mirrors the condition in humans, than when transfected alone, so the mutant protein could be stabilised in the presence of wildtype eEF1A2. I used CRISPR on LUHMES cells to make a mutant neuronal cell line containing the D252H mutation in eEF1A2. Due to time restraints no phenotypic differences between the wild type line and the D252H mutation line have yet been identified, but would form the focus of a future project.
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Griffiths, Lowri Ann. "Investigating the role of eEF1A2 in motor neuron degeneration." Thesis, University of Edinburgh, 2011. http://hdl.handle.net/1842/5924.

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Анотація:
Abnormal expression of the eukaryotic translation elongation factor 1A (eEF1A) has been implicated in disease states such as motor neuron degeneration and cancer. Two variants of eEF1A are found in mammals, named eEF1A1 and eEF1A2. These two variants are encoded by different genes, produce proteins which are 92% identical but have very different patterns of expression. eEF1A1 is almost ubiquitously expressed while eEF1A2 is expressed only in specialised cell types such as motor neurons and muscle. A spontaneous mutation in eEF1A2 results in the wasted mouse phenotype which shows similar characteristics in the mouse to those seen in human motor neuron degeneration. This mutation has been shown to be a 15.8kb deletion resulting in the complete loss of the promoter region and first non coding exon of eEF1A2 which completely abolishes protein expression. The main aim of this project was to further investigate the role of eEF1A2 in motor neuron degeneration. Firstly, although the wasted phenotype is considered to be caused by a recessive mutation, I established a cohort of aged heterozygote mice to evaluate whether any changes are seen later in life that might model late onset motor neuron degeneration. A combination of behavioural tests and pathology was used to compare wild type and heterozygous mice up to 21 months of age. Whilst results indicate that there is no significant difference between ageing heterozygotes and wildtype controls, there is an indication that female heterozygote mice perform slightly worse that wildtype controls on the rotarod (a behavioural test for motor function). Secondly, I aimed to investigate the primary cause of the wasted pathology by generating transgenic wasted mice expressing neuronal eEF1A2 only. This would complement previous experiments in the lab which studied transgenic wasted mice expressing eEF1A2 in muscle only. Unfortunately the expression of eEF1A2 in the transgenic animals was not neuronal specific. However a transgenic line with expression of eEF1A2 in neurons and skeletal muscle but not cardiac muscle has been generated which clearly warrants further investigation. Thirdly, I wished to assess whether eEF1A2 has any role in human motor neuron degeneration. To achieve this, eEF1A2 expression was investigated in spinal cords from human motor neuron disease (MND) patients. Preliminary data suggests that motor neurons from some MND patients express significantly less eEF1A2 than motor neurons of control samples. Further work is required to confirm these findings. Finally, I investigated the individual roles of eEF1A1 and eEF1A2 in the heat shock response. I used RNAi to ablate each variant separately in cells and subsequently measured the ability of each variant individually to mount a heat shock response. Results indicate a clear role for eEF1A1 but not eEF1A2 in the induction of heat shock. This may explain in part why motor neurons exhibit a poor heat shock response as they express eEF1A2 and not eEF1A1. These experiments shed light on our understanding of the role of eEF1A2 in motor neuron degeneration and uncover many new avenues of future investigation.
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5

Többen, Udo [Verfasser]. "A novel function for the eukaryotic translation elongation factor 1A / presented by Udo Többen." 2004. http://d-nb.info/972338101/34.

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Liao, Ts'ai-Lien, and 廖彩蓮. "Molecular Cloning Of The Ribosomal Protein, S17 And L37, And The Elongation Factor 1a Of Carp And Their Expression During Oocyte Development." Thesis, 1999. http://ndltd.ncl.edu.tw/handle/27737268127188154843.

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Анотація:
碩士
國立臺灣大學
動物學研究所
87
Carp elongation factor 1α( EF-1α) and ribosomal proteins( L37 and S17) were isolated from an ovary cDNA library. EF-1α is a 1651bp cDNA and encodes a 458 residue polypeptide. L37 is a 389bp cDNA and encodes 92 residue polypeptide. S17 is a 434bp cDNA and encodes 135 residue polypeptide. They are extremely high homologous to their counterparts in other animals. In this paper, I study the expression change of EF-1α, L37 and S17 during the oogenesis to understand the translation during development of carp oocyte. Northern blotting revealed that EF-1α, L37 and S17 mRNA reach the highest level in the second stage of oogenesis, but they decrease with the oocyte maturation. Western blot analysis indicated that EF-1αprotein is accumulated until the second stage and then decreases. However, it failed to detect L37 and S17 proteins in oocytes by antiserum against bacterial recombinant L37 and S17 proteins.
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Leclercq, Tamara Marie. "Regulation of sphingosine kinase by interacting proteins." Thesis, 2010. http://hdl.handle.net/2440/64752.

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Sphingosine kinase 1 (SK1) is responsible for phosphorylating the lipid sphingosine, generating the bio-active phospholipid, sphingosine 1-phosphate (S1P). Cells possess basal SK1 activity which has been proposed to serve in a ‘housekeeping’ function to limit the levels of proapoptotic sphingosine and ceramide in the cell. In some circumstances, however, such as cell exposure to growth factors and cytokines this basal level of SK1 activity is increased, resulting in an increased production of S1P. As S1P is a pro-proliferative, pro-survival molecule, its increased production is associated with enhanced cell proliferation, survival and an oncogenic phenotype. The Pitson laboratory has shown previously that one mechanism by which SK1 is activated is through phosphorylation at Ser-225 by ERK1/2. Here, my studies focused on alternative mechanisms of SK1 activation that arise through its interaction with two proteins, eukaryotic elongation factor 1A (eEF1A) and a relatively uncharacterised protein, SK activator molecule 1 (SKAM). eEF1A is able to directly increase the catalytic activity of SK1 in vitro and is also able to increase endogenous SK activity when over-expressed in quiescent cells that have reduced levels of endogenous eEF1A protein. Due to the abundance of eEF1A protein within a cell, I hypothesized that the effect of eEF1A on SK activity may be dynamically regulated. eEF1A contains a ‘G protein-like’ domain that enables it to bind GDP and GTP. When bound by GTP, eEF1A undergoes a large conformational change that enables it to bind aminoacyltRNA for transport to the ribosome. Similarly, just as the nucleotide-bound state of eEF1A regulates its role in protein synthesis, I found that the nucleotide-bound state of eEF1A also regulates its ability to activate SK1. Strikingly, it is only the translationally inactive eEF1A.GDP that can activate SK1. A truncated form of eEF1A named PTI-1 has been described that lacks the ‘G protein-like’ domain and thus can not bind guanine nucleotides, rendering it structurally analogous to eEF1A.GDP. In keeping with my finding that only eEF1A.GDP activates SK1, I found that PTI-1 also activates SK1 both in vitro and in cells. Importantly, PTI-1 has been previously characterized as an oncoprotein and for the first time my studies have shown a likely mechanism by which PTI-1 induces a tumourigenic phenotype. Expression of PTI-1 in NIH 3T3 cells induces neoplastic transformation, as measured by focus formation. Notably, this PTI-1-induced transformation is blocked when cells are treated with SK inhibitors or when cells are co-transfected with PTI-1 and a dominant negative SK1, indicating that oncogenesis by PTI-1 is mediated through SK1. The current study also investigated the regulation of SK1 activity by its interaction with SKAM1. Previous studies have shown that SKAM1, like eEF1A, can directly increase the catalytic activity of SK1 in vitro and in cells. My studies have determined the minimal region of interaction of SKAM1 that is still able to interact with and activate SK1. Remarkably, a 35 amino acid SKAM1 peptide retained the ability to activate SK1. The physiological relevance of the SK1-SKAM1 interaction was also examined and I have shown that knock-down of SKAM1, and the related protein SKAM2, in HEK 293T cells resulted in decreased cell proliferation coupled with increased susceptibility to apoptosis. Results presented here, also suggest that phosphorylation of SKAM1 at Tyr-46 acts as a negative regulator for SKAM1-induced SK1 activation. In summary, the current study presents two novel SK1 interacting proteins that directly increase the catalytic activity of this enzyme, and investigates mechanisms by which their effects on SK1 activity are regulated. While the guanine nucleotide bound state of eEF1A1 determines its effects on SK1 activity, the phosphorylation status of SKAM1 appears to determine its ability to activate SK1.
Thesis (Ph.D.) -- University of Adelaide, School of Molecular and Biomedical Science, 2010
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Частини книг з теми "Elongation factor 1A"

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Migliaccio, Nunzia, Gennaro Sanità, Immacolata Ruggiero, Nicola M. Martucci, Carmen Sanges, Emilia Rippa, Vincenzo Quagliariello, Ferdinando Papale, Paolo Arcari, and Annalisa Lamberti. "Cellular Interaction of Human Eukaryotic Elongation Factor 1A Isoforms." In Protein-Protein Interaction Assays. InTech, 2018. http://dx.doi.org/10.5772/intechopen.74733.

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Gorodetskiy, Vadim. "Felty’s Syndrome." In Rare Diseases [Working Title]. IntechOpen, 2021. http://dx.doi.org/10.5772/intechopen.97080.

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Felty’s syndrome (FS) is an uncommon subset of seropositive rheumatoid arthritis (RA) complicated by neutropenia with or without splenomegaly. The pathogenesis of neutropenia in FS is still not fully understood, but it is believed that the principal cause is neutrophil survival defect. Autoantibodies against peptidylarginine deiminase type 4 deiminated histones, glucose-6-phosphate isomerase, and eukaryotic elongation factor 1A-1 antigen may contribute to neutropenia development in FS patients. Splenic histology in FS shows non-specific findings and spleen size do not correlate with neutropenia. Cases of T-cell large granular lymphocytic leukemia with low tumor burden in blood and concomitant RA are clinically indistinguishable from FS and present a diagnostic challenge. Examination of T-cell clonality, mutations in signal transducer and activator of transcription 3 gene, and the number of large granular lymphocytes in the blood can establish a correct diagnosis. Optimal approaches to therapy for FS have not been developed, but the use of rituximab seems promising. In this chapter, the epidemiology, pathogenesis, clinical manifestations, differential diagnosis, and treatment options for FS are discussed.
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